Evidence map›Paper›PMID 19716792›Full record

ArticleMolecular cell2009

Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation.

Michael E Budiman, Jodi L Bubenik, Angela C Miniard, Lisa M Middleton, Carri A Gerber, Ayla Cash, Donna M Driscoll

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
8.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed, 125 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. RNA-Binding Proteins (RBPs) and Circular RNA Biogenesis.Advances in experimental medicine and biology · 2025
    Review
  6. Article
  7. Review
  8. Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. The Effect of tRNAInternational journal of molecular sciences · 2021
    Article
  15. Review
  16. SECISBP2 is a novel prognostic predictor that regulates selenoproteins in diffuse large B-cell lymphoma.Laboratory investigation; a journal of technical methods and pathology · 2021
    Article
  17. Article
  18. Review
  19. Review
  20. Review

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Michael E BudimanDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Jodi L Bubenik
Angela C Miniard
Lisa M Middleton
Carri A Gerber
Ayla Cash
Donna M Driscoll
Cleveland Clinic Lerner College of Medicine · USCase Western Reserve University · USThe Ohio State University · US

Funding

Regulation of Selenoprotein Synthesis by SECIS-binding ProteinsR01DK078591 · NIDDK · CLEVELAND CLINIC LERNER COM-CWRU · PI DRISCOLL, DONNA M · 2007 to 2014
$2.6M
An unexpected role for elF4a3 in regulating GPx1 selenoprotein expressionF32DK083154 · NIDDK · CLEVELAND CLINIC LERNER COM-CWRU · PI BUDIMAN, MICHAEL EVEREST · 2008 to 2010
$148k
NIDDK NIH HHS F32 DK083154NIDDK NIH HHS R01 DK078591
6 · The paper itself

Abstract

The synthesis of selenoproteins requires the translational recoding of the UGA stop codon as selenocysteine. During selenium deficiency, there is a hierarchy of selenoprotein expression, with certain selenoproteins synthesized at the expense of others. The mechanism by which the limiting selenocysteine incorporation machinery is preferentially utilized to maintain the expression of essential selenoproteins has not been elucidated. Here we demonstrate that eukaryotic initiation factor 4a3 (eIF4a3) is involved in the translational control of a subset of selenoproteins. The interaction of eIF4a3 with the selenoprotein mRNA prevents the binding of SECIS binding protein 2, which is required for selenocysteine insertion, thereby inhibiting the synthesis of the selenoprotein. Furthermore, the expression of eIF4a3 is regulated in response to selenium. Based on knockdown and overexpression studies, eIF4a3 is necessary and sufficient to mediate selective translational repression in cells. Our results support a model in which eIF4a3 links selenium status with differential selenoprotein expression.

Indexed as

Protein Modification, Translational3' Untranslated RegionsAnimalsBinding SitesCell Line, TumorCodon, TerminatorDEAD-box RNA HelicasesEnzyme InductionEukaryotic Initiation Factor-4AGlutathione PeroxidaseGlutathione Peroxidase GPX1HomeostasisMolecular WeightNucleic Acid ConformationPhospholipid Hydroperoxide Glutathione PeroxidaseRats3' Untranslated RegionsCodon, TerminatorDEAD-box RNA HelicasesEukaryotic Initiation Factor-4AGlutathione PeroxidaseGlutathione Peroxidase GPX1Gpx1 protein, ratPhospholipid Hydroperoxide Glutathione PeroxidaseRNA-Binding ProteinsRNA, MessengerSecisbp2 protein, ratSelenbp1 protein, ratSeleniumSelenium-Binding ProteinsSelenocysteineSelenoproteins

Identifiers

PMID19716792
PMCPMC2752292
OpenAlexW2003018523

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.